Home > Publications database > Der Lysinexportcarrier in Corynebacterium glutamicum - Topologie und Regulation |
Dissertation / PhD Thesis/Book | PreJuSER-26977 |
2000
Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag
Jülich
Please use a persistent id in citations: http://hdl.handle.net/2128/20603
Report No.: Juel-3755
Abstract: The L-Iysine export carrier LysE of the Gram-positive bacterium Corynebacterium gIptamisum represents the firnt funetionally analysed member of a new widespread superfamily of bacterial translocators . The results of phoA and IacZ fusion analysis of the topology of LysE suggest a unique topology for LysE . There is good evidence supporting a model in which LysE spans the cytoplasmic membrane five times with one additional hydrophobic domain which is most probably attached to the external side of the cytoplasmic membranei The putative regulator gene LysG is located adjacent to lysE and is divergently transcribed. Single-copy transcriptional fusions of lysE with lacZ show that LysG is a positive regulator of lysE expression enabling it to be induced up to 20-fold . This induction requires an inducer molecule . Using dipeptide feeding experiments intracellular L-Iysine, L-arginine, L-citrulline and L-histidine were shown to act as inducers an the LysG-mediated lysE expression . White L-arginine and L-Iysine are substrates of LysE this is not the oase for L-histidine and Lcitrulline . An in vivo experiment and gel shift studies provided evidence that LysG binds to the intergenic region of lysE and LysG. This region was delimited to 105 bp of this divergent promoter region of lysE and lysG .
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